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Database: UniProt
Entry: A9WS59_RENSM
LinkDB: A9WS59_RENSM
Original site: A9WS59_RENSM 
ID   A9WS59_RENSM            Unreviewed;      1013 AA.
AC   A9WS59;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:ABY24188.1};
DE            EC=2.7.7.42 {ECO:0000313|EMBL:ABY24188.1};
GN   OrderedLocusNames=RSal33209_2462 {ECO:0000313|EMBL:ABY24188.1};
OS   Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS   NBRC 15589 / NCIMB 2235).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Renibacterium.
OX   NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY24188.1, ECO:0000313|Proteomes:UP000002007};
RN   [1] {ECO:0000313|Proteomes:UP000002007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC   {ECO:0000313|Proteomes:UP000002007};
RX   PubMed=18723615; DOI=10.1128/JB.00721-08;
RA   Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA   Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA   Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT   "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT   reductive evolution away from an environmental Arthrobacter ancestor.";
RL   J. Bacteriol. 190:6970-6982(2008).
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DR   EMBL; CP000910; ABY24188.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9WS59; -.
DR   STRING; 288705.RSal33209_2462; -.
DR   KEGG; rsa:RSal33209_2462; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_1_0_11; -.
DR   OMA; EFMVQYA; -.
DR   Proteomes; UP000002007; Chromosome.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd05401; NT_GlnE_GlnD_like; 2.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 2.
DR   InterPro; IPR023057; GlnE.
DR   InterPro; IPR005190; GlnE_rpt_dom.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   PANTHER; PTHR30621:SF0; BIFUNCTIONAL GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE/ADENYLYL-REMOVING ENZYME; 1.
DR   PANTHER; PTHR30621; GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF08335; GlnD_UR_UTase; 2.
DR   Pfam; PF03710; GlnE; 2.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR   SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000313|EMBL:ABY24188.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:ABY24188.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002007};
KW   Transferase {ECO:0000313|EMBL:ABY24188.1}.
FT   DOMAIN          88..337
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          361..505
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          610..846
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          871..1010
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   1013 AA;  110505 MW;  278D7EB4248D898E CRC64;
     MGQATMVKSL PRVLIEQGFA DLEKSTRFLA VPELLDFAQD DLFAGLAFAA DPDLALQSLV
     RMLAAPAELA ERVARLVQAG PKRSEPMFRL LGASEALADF LIRNPGQSAA LEISVSAEPV
     GVPGKVLRTS LLQAVGADPE SATPLSGLGT AEATTAMRRQ YRRHLTELAI RDLCAADPAD
     VLPIVAAELA DLAGAALDAA LAIARAELVG TFSAQQVTAV ELAVIGMGKC GARELNYISD
     VDVIYVVAAN GLADYDELPI QVGTQLAALL ARIINAPDRE PGLWELDANL RPEGKDGPLV
     RTLDSHLEYY RRWASSWEFQ ALLKARPIAG NLALGEQYTS ALAPMIWNSS ERDGFVESVQ
     AMRRRVSANI PAEEQNRQLK LGPGGLRDVE FTVQLLQLVH GKADSSLRKQ DTTGAIEALS
     TAGYVGRTDA AEFDGAYRYL RVLEHRIQLV HLRRTHLMPV AEPALRALAR SSQGAMAMSR
     PSAKVLLDQW QSVKRRVRSL HERIFYRPLL NAAANLSAED ASLSPESAQA RLAALGYQDT
     AGAMRHIEAL TTGVSRRAAL QRQLLPVLLD WLGDGVDPDS GLLAFRRLSE SLGTTHWYLG
     MLRDSQAAAE RLCHVLSSSH LIADLLEVSP EETKWLGSDK DLRPLSFQAQ WQEIQSKMSR
     HPDPSSAMRL IRLIRRREVL RIALADSAGL LDQDAIGTAL GDVDRAAVLG ALHVAENQQD
     EAKTDVLVVA MGRQGGREIG YGSDADVLFV HKARPGVDPA GAQAQAVQIV SQLSALLTQP
     LKPAIRAERV LAIDADLRPE GKNGALVRSL DSYREYYGRW SLIWEAQALL RARPMAGSDE
     LAAEFMALVD SVRYPDQLSE QDLREVRRVK ARVESERLPR GADPARQIKL GRGGLSDVEW
     LVQLLQLQHA RAQVQLRTTS TLTALSGLAE LGFVADEDAD ALAKAWRLAS RIRSANVLWT
     GRGSDSLPSS RRDLEAVARW CGYPPGHGGA FEEDYLRITR QARAVFERLF YGE
//
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